Time value - Revision history

en>Vanisaac: Undid revision 612835493 by Vanisaac (talk) wrong "TV"

2014-06-14T01:09:35Z

Undid revision 612835493 by Vanisaac (talk) wrong "TV"

← Older revision		Revision as of 03:09, 14 June 2014
Line 1:		Line 1:
	~~{{PBB\|geneid=5406}}~~		Nothing to write about me really.<br>Hurrey Im here and a member of wmflabs.org.<br>I really wish I'm useful at all<br><br>Review my web-site: [http://dawonls.dothome.co.kr/db/?document_srl=294320 http://www.hostgator1centcoupon.info/]
	'''Pancreatic lipase''', also known as '''pancreatic triacylglycerol lipase''', is secreted from the [[pancreas]], and is the primary [[lipase]] ([[enzyme]]) that [[hydrolyzes]] (breaks down) dietary [[fat]] [[molecules]] in the human digestive system, converting [[triglyceride]] substrates found in ingested oils to ~~[[monoglyceride]]s and [[free fatty acid]]s~~.

	~~:Triacylglycerol + 2 H<sub>2</sub>O <math>\rightleftharpoons~~<~~/math~~> ~~2-monoacylglycerol + 2 fatty acid anions~~

	[[Bile salts]] secreted from the [[liver]] and stored in [[gallbladder]] are released into the [[duodenum]] where they coat and emulsify large fat droplets into smaller droplets, thus increasing the overall [[surface area]] of the fat, which allows the lipase to break apart the fat more effectively. The resulting [[monomers]] (2 free fatty acids and ~~one 2-monoacylglycerol) are then moved by way of [[peristalsis]] along the [[small intestine]] to be absorbed into the [[lymphatic system]] by a specialized vessel called~~ a ~~[[lacteal]]. This protein belongs to [[pancreatic lipase family]].~~

	~~Unlike some pancreatic enzymes that are activated by [[proteolytic cleavage]] (e.g. [[trypsinogen]]), pancreatic lipase is secreted in its final form. However it only becomes efficient in the presence~~ of ~~[[colipase]] in the [[duodenum]]~~.

	~~In humans, pancreatic lipase is encoded by the '''PNLIP''' [[gene]]~~.<~~ref name="pmid1783385"~~>~~{{cite journal \| author = Davis RC, Diep A, Hunziker W, Klisak~~ I, Mohandas T, Schotz MC, Sparkes RS, Lusis AJ \| title = Assignment of human pancreatic lipase gene (PNLIP) to chromosome 10q24-q26 \| journal = Genomics \| volume = 11 \| issue = 4 \| pages = 1164–6 \|date=December 1991 \| pmid = 1783385 \| doi = 10.1016/0888-7543(91)90048-J\| url = \| issn = }}<~~/ref~~><~~ref name="entrez"~~>~~{{cite~~ web ~~\| title = Entrez Gene~~: ~~pancreatic lipase\| url =~~ http://~~www~~.~~ncbi~~.~~nlm~~.~~nih.gov~~/~~sites~~/~~entrez~~?Db=~~gene&Cmd=ShowDetailView&TermToSearch=5406\| accessdate = }}</ref>~~

	~~== Diagnostic importance ==~~
	Pancreatic lipase is secreted into the [[duodenum]] through the duct system of the pancreas. Normally its concentration in serum is very low. Under extreme disruption of pancreatic function, such as [[pancreatitis]] or [[pancreatic cancer\|pancreatic adenocarcinoma]], the pancreas may begin to [[autolysis\|autolyse]] and release pancreatic enzymes including pancreatic lipase into serum. Thus, through measurement of serum concentration of pancreatic lipase, acute pancreatitis can be diagnosed.<ref name="pmid6207965">{{cite journal \| author = Koop H \| title = Serum levels of pancreatic enzymes and their clinical significance \| journal = Clin Gastroenterol \| volume = 13 \| issue = 3 \| pages = 739–61 \|date=September 1984 \| pmid = 6207965 \| doi = \| url = \| issn = }}</ref>

	~~==See also==~~
	* [[Orlistat]] (a pancreatic lipase inhibitor marketed as an anti-[[obesity]] medication)

	~~== References ==~~
	~~{{Reflist}}~~

	~~==Further reading==~~
	~~{{refbegin \| 2}}~~
	*{{cite journal \|author=Crandall WV, Lowe ME \|title=Colipase residues Glu64 and Arg65 are essential for normal lipase-mediated fat digestion in the presence of bile salt micelles. \|journal=J. Biol. Chem. \|volume=276 \|issue= 16 \|pages= 12505–12 \|year= 2001 \|pmid= 11278590 \|doi= 10.1074/jbc.M009986200 }}
	*{{cite journal \|author=Freie AB, Ferrato F, CarriÃ¨re F, Lowe ME \|title=Val-407 and Ile-408 in the beta5'-loop of pancreatic lipase mediate lipase-colipase interactions in the presence of bile salt micelles. \|journal=J. Biol. Chem. \|volume=281 \|issue= 12 \|pages= 7793–800 \|year= 2006 \|pmid= 16431912 \|doi= 10.1074/jbc.M512984200 }}
	*{{cite journal \|author=Hegele RA, Ramdath DD, Ban MR, ''et al.'' \|title=Polymorphisms in PNLIP, encoding pancreatic lipase, and associations with metabolic traits. \|journal=J. Hum. Genet. \|volume=46 \|issue= 6 \|pages= 320–4 \|year= 2001 \|pmid= 11393534 \|doi= 10.1007/s100380170066 }}
	*{{cite journal \|author=Chahinian H, Sias B, CarriÃ¨re F \|title=The C-terminal domain of pancreatic lipase: ~~functional and structural analogies with c2 domains. \|journal=Curr. Protein Pept. Sci. \|volume=1 \|issue= 1 \|pages= 91–103 \|year= 2000 \|pmid= 12369922 \|doi= }}~~
	*{{cite journal \|author=Ranaldi S, Belle V, Woudstra M, ''et al.'' \|title=Lid opening and unfolding in human pancreatic lipase at low pH revealed by site-directed spin labeling EPR and FTIR spectroscopy. \|journal=Biochemistry \|volume=48 \|issue= 3 \|pages= 630–8 \|year= 2009 \|pmid= 19113953 \|doi= 10.1021/~~bi801250s }}~~
	*{{cite journal \|author=Grupe A, Li Y, Rowland C, ''et al.'' \|title=A scan of chromosome 10 identifies a novel locus showing strong association with late-onset Alzheimer disease. \|journal=Am. J. Hum. Genet. \|volume=78 \|issue= 1 \|pages= 78–88 \|year= 2006 \|pmid= 16385451 \|doi= 10.1086/~~498851 \|pmc=1380225}}~~
	*{{cite journal \|author=Thomas A, Allouche M, Basyn F, ''et al.'' \|title=Role of the lid hydrophobicity pattern in pancreatic lipase activity. \|journal=J. Biol. Chem. \|volume=280 \|issue= 48 \|pages= 40074–83 \|year= 2005 \|pmid= 16179352 \|doi= 10.1074/jbc.M502123200 }}
	*{{cite journal \|author=van Tilbeurgh H, Egloff MP, Martinez C, ''et al.'' \|title=Interfacial activation of the lipase-procolipase complex by mixed micelles revealed by X-ray crystallography. \|journal=Nature \|volume=362 \|issue= 6423 \|pages= 814–20 \|year= 1993 \|pmid= 8479519 \|doi= 10.1038/362814a0 }}
	*{{cite journal \|author=Lessinger JM, Arzoglou P, Ramos P, ''et al.'' \|title=Preparation and characterization of reference materials for human pancreatic lipase: BCR 693 (from human pancreatic juice) and BCR 694 (recombinant). \|journal=Clin. Chem. Lab. Med. \|volume=41 \|issue= 2 \|pages= 169–76 \|year= 2003 \|pmid= 12667003 \|doi= 10.1515/CCLM.2003.028 }}
	*{{cite journal \|author=Colin DY, Deprez-Beauclair P, Allouche M, ''et al.'' \|title=Exploring the active site cavity of human pancreatic lipase. \|journal=Biochem. Biophys. Res. Commun. \|volume=370 \|issue= 3 \|pages= 394–8 \|year= 2008 \|pmid= 18353248 \|doi= 10.1016/j.bbrc.2008.03.043 }}
	*{{cite journal \|author=Ramos P, Coste T, PiÃ©mont E, ''et al.'' \|title=Time-resolved fluorescence allows selective monitoring of Trp30 environmental changes in the seven-Trp-containing human pancreatic lipase. \|journal=Biochemistry \|volume=42 \|issue= 43 \|pages= 12488–96 \|year= 2003 \|pmid= 14580194 \|doi= 10.1021/bi034900e }}
	*{{cite journal \|author=Yang Y, Lowe ME \|title=Human pancreatic triglyceride lipase expressed in yeast cells: purification and characterization. \|journal=Protein Expr. Purif. \|volume=13 \|issue= 1 \|pages= 36–40 \|year= 1998 \|pmid= 9631512 \|doi= 10.1006/prep.1998.0874 }}
	*{{cite journal \|author=Sims HF, Jennens ML, Lowe ME \|title=The human pancreatic lipase-encoding gene: structure and conservation of an Alu sequence in the lipase gene family. ~~\|journal=Gene \|volume=131 \|issue= 2 \|pages= 281–5 \|year= 1993 \|pmid= 8406023 \|doi= 10~~.~~1016~~/~~0378-1119(93)90307-O}}~~
	*{{cite journal \|author=Grandval P, De Caro A, De Caro J, ''et al.'' \|title=Critical evaluation of a specific ELISA and two enzymatic assays of pancreatic lipases in human sera. \|journal=Pancreatology \|volume=4 \|issue= 6 \|pages= 495-503; discussion 503-4 \|year= 2004 \|pmid= 15316225 \|doi= 10.1159/000080246 }}
	*{{cite journal \|author=Belle V, Fournel A, Woudstra M, ''et al.'' \|title=Probing the opening of the pancreatic lipase lid using site-directed spin labeling and EPR spectroscopy. \|journal=Biochemistry \|volume=46 \|issue= 8 \|pages= 2205–14 \|year= 2007 \|pmid= 17269661 \|doi= 10.1021/bi0616089 }}
	*{{cite journal \|author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' \|title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). \|journal=Genome Res. \|volume=14 \|issue= 10B \|pages= 2121–7 \|year= 2004 \|pmid= 15489334 \|doi= 10.1101/gr.2596504 \|pmc=528928}}
	*{{cite journal \|author=Lowe ME \|title=Structure and function of pancreatic lipase and colipase. \|journal=Annu. Rev. Nutr. \|volume=17 \|issue= \|pages= 141–58 \|year= 1997 \|pmid= 9240923 \|doi= 10.1146/annurev.nutr.17.1.141 }}
	*{{cite journal \|author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' \|title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. \|journal=Proc. Natl. Acad. Sci. U.S.A. \|volume=99 \|issue= 26 \|pages= 16899–903 \|year= 2002 \|pmid= 12477932 \|doi= 10.1073/pnas.242603899 \|pmc=139241}}
	*{{cite journal \|author=Bourbon-Freie A, Dub RE, Xiao X, Lowe ME \|title=Trp-107 and trp-253 account for the increased steady state fluorescence that accompanies the conformational change in human pancreatic triglyceride lipase induced by tetrahydrolipstatin and bile salt. \|journal=J. Biol. Chem. \|volume=284 \|issue= 21 \|pages= 14157–64 \|year= 2009 \|pmid= 19346257 \|doi= 10.1074/jbc.M901154200 }}
	*{{cite journal \|author=Ranaldi S, Belle V, Woudstra M, ''et al.'' \|title=Amplitude of pancreatic lipase lid opening in solution and identification of spin label conformational subensembles by combining continuous wave and pulsed EPR spectroscopy and molecular dynamics. \|journal=Biochemistry \|volume=49 \|issue= 10 \|pages= 2140–9 \|year= 2010 \|pmid= 20136147 \|doi= 10.1021/bi901918f }}
	~~{{refend}}~~

	~~{{PDB Gallery\|geneid=5406}}~~
	~~{{Esterases}}~~
	~~{{Clinical biochemistry blood tests}}~~

	~~[[Category:EC 3.1.1]~~]

en>Matthiaspaul: Improved some entries

2012-10-04T01:21:43Z

Improved some entries

New page

{{PBB|geneid=5406}}
'''Pancreatic lipase''', also known as '''pancreatic triacylglycerol lipase''', is secreted from the [[pancreas]], and is the primary [[lipase]] ([[enzyme]]) that [[hydrolyzes]] (breaks down) dietary [[fat]] [[molecules]] in the human digestive system, converting [[triglyceride]] substrates found in ingested oils to [[monoglyceride]]s and [[free fatty acid]]s.

:Triacylglycerol + 2 H<sub>2</sub>O <math>\rightleftharpoons</math> 2-monoacylglycerol + 2 fatty acid anions

[[Bile salts]] secreted from the [[liver]] and stored in [[gallbladder]] are released into the [[duodenum]] where they coat and emulsify large fat droplets into smaller droplets, thus increasing the overall [[surface area]] of the fat, which allows the lipase to break apart the fat more effectively. The resulting [[monomers]] (2 free fatty acids and one 2-monoacylglycerol) are then moved by way of [[peristalsis]] along the [[small intestine]] to be absorbed into the [[lymphatic system]] by a specialized vessel called a [[lacteal]]. This protein belongs to [[pancreatic lipase family]].

Unlike some pancreatic enzymes that are activated by [[proteolytic cleavage]] (e.g. [[trypsinogen]]), pancreatic lipase is secreted in its final form. However it only becomes efficient in the presence of [[colipase]] in the [[duodenum]].

In humans, pancreatic lipase is encoded by the '''PNLIP''' [[gene]].<ref name="pmid1783385">{{cite journal | author = Davis RC, Diep A, Hunziker W, Klisak I, Mohandas T, Schotz MC, Sparkes RS, Lusis AJ | title = Assignment of human pancreatic lipase gene (PNLIP) to chromosome 10q24-q26 | journal = Genomics | volume = 11 | issue = 4 | pages = 1164–6 |date=December 1991 | pmid = 1783385 | doi = 10.1016/0888-7543(91)90048-J| url = | issn = }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: pancreatic lipase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5406| accessdate = }}</ref>

== Diagnostic importance ==
Pancreatic lipase is secreted into the [[duodenum]] through the duct system of the pancreas. Normally its concentration in serum is very low. Under extreme disruption of pancreatic function, such as [[pancreatitis]] or [[pancreatic cancer|pancreatic adenocarcinoma]], the pancreas may begin to [[autolysis|autolyse]] and release pancreatic enzymes including pancreatic lipase into serum. Thus, through measurement of serum concentration of pancreatic lipase, acute pancreatitis can be diagnosed.<ref name="pmid6207965">{{cite journal | author = Koop H | title = Serum levels of pancreatic enzymes and their clinical significance | journal = Clin Gastroenterol | volume = 13 | issue = 3 | pages = 739–61 |date=September 1984 | pmid = 6207965 | doi = | url = | issn = }}</ref>

==See also==
* [[Orlistat]] (a pancreatic lipase inhibitor marketed as an anti-[[obesity]] medication)

== References ==
{{Reflist}}

==Further reading==
{{refbegin | 2}}
*{{cite journal |author=Crandall WV, Lowe ME |title=Colipase residues Glu64 and Arg65 are essential for normal lipase-mediated fat digestion in the presence of bile salt micelles. |journal=J. Biol. Chem. |volume=276 |issue= 16 |pages= 12505–12 |year= 2001 |pmid= 11278590 |doi= 10.1074/jbc.M009986200 }}
*{{cite journal |author=Freie AB, Ferrato F, CarriÃ¨re F, Lowe ME |title=Val-407 and Ile-408 in the beta5'-loop of pancreatic lipase mediate lipase-colipase interactions in the presence of bile salt micelles. |journal=J. Biol. Chem. |volume=281 |issue= 12 |pages= 7793–800 |year= 2006 |pmid= 16431912 |doi= 10.1074/jbc.M512984200 }}
*{{cite journal |author=Hegele RA, Ramdath DD, Ban MR, ''et al.'' |title=Polymorphisms in PNLIP, encoding pancreatic lipase, and associations with metabolic traits. |journal=J. Hum. Genet. |volume=46 |issue= 6 |pages= 320–4 |year= 2001 |pmid= 11393534 |doi= 10.1007/s100380170066 }}
*{{cite journal |author=Chahinian H, Sias B, CarriÃ¨re F |title=The C-terminal domain of pancreatic lipase: functional and structural analogies with c2 domains. |journal=Curr. Protein Pept. Sci. |volume=1 |issue= 1 |pages= 91–103 |year= 2000 |pmid= 12369922 |doi= }}
*{{cite journal |author=Ranaldi S, Belle V, Woudstra M, ''et al.'' |title=Lid opening and unfolding in human pancreatic lipase at low pH revealed by site-directed spin labeling EPR and FTIR spectroscopy. |journal=Biochemistry |volume=48 |issue= 3 |pages= 630–8 |year= 2009 |pmid= 19113953 |doi= 10.1021/bi801250s }}
*{{cite journal |author=Grupe A, Li Y, Rowland C, ''et al.'' |title=A scan of chromosome 10 identifies a novel locus showing strong association with late-onset Alzheimer disease. |journal=Am. J. Hum. Genet. |volume=78 |issue= 1 |pages= 78–88 |year= 2006 |pmid= 16385451 |doi= 10.1086/498851 |pmc=1380225}}
*{{cite journal |author=Thomas A, Allouche M, Basyn F, ''et al.'' |title=Role of the lid hydrophobicity pattern in pancreatic lipase activity. |journal=J. Biol. Chem. |volume=280 |issue= 48 |pages= 40074–83 |year= 2005 |pmid= 16179352 |doi= 10.1074/jbc.M502123200 }}
*{{cite journal |author=van Tilbeurgh H, Egloff MP, Martinez C, ''et al.'' |title=Interfacial activation of the lipase-procolipase complex by mixed micelles revealed by X-ray crystallography. |journal=Nature |volume=362 |issue= 6423 |pages= 814–20 |year= 1993 |pmid= 8479519 |doi= 10.1038/362814a0 }}
*{{cite journal |author=Lessinger JM, Arzoglou P, Ramos P, ''et al.'' |title=Preparation and characterization of reference materials for human pancreatic lipase: BCR 693 (from human pancreatic juice) and BCR 694 (recombinant). |journal=Clin. Chem. Lab. Med. |volume=41 |issue= 2 |pages= 169–76 |year= 2003 |pmid= 12667003 |doi= 10.1515/CCLM.2003.028 }}
*{{cite journal |author=Colin DY, Deprez-Beauclair P, Allouche M, ''et al.'' |title=Exploring the active site cavity of human pancreatic lipase. |journal=Biochem. Biophys. Res. Commun. |volume=370 |issue= 3 |pages= 394–8 |year= 2008 |pmid= 18353248 |doi= 10.1016/j.bbrc.2008.03.043 }}
*{{cite journal |author=Ramos P, Coste T, PiÃ©mont E, ''et al.'' |title=Time-resolved fluorescence allows selective monitoring of Trp30 environmental changes in the seven-Trp-containing human pancreatic lipase. |journal=Biochemistry |volume=42 |issue= 43 |pages= 12488–96 |year= 2003 |pmid= 14580194 |doi= 10.1021/bi034900e }}
*{{cite journal |author=Yang Y, Lowe ME |title=Human pancreatic triglyceride lipase expressed in yeast cells: purification and characterization. |journal=Protein Expr. Purif. |volume=13 |issue= 1 |pages= 36–40 |year= 1998 |pmid= 9631512 |doi= 10.1006/prep.1998.0874 }}
*{{cite journal |author=Sims HF, Jennens ML, Lowe ME |title=The human pancreatic lipase-encoding gene: structure and conservation of an Alu sequence in the lipase gene family. |journal=Gene |volume=131 |issue= 2 |pages= 281–5 |year= 1993 |pmid= 8406023 |doi= 10.1016/0378-1119(93)90307-O}}
*{{cite journal |author=Grandval P, De Caro A, De Caro J, ''et al.'' |title=Critical evaluation of a specific ELISA and two enzymatic assays of pancreatic lipases in human sera. |journal=Pancreatology |volume=4 |issue= 6 |pages= 495-503; discussion 503-4 |year= 2004 |pmid= 15316225 |doi= 10.1159/000080246 }}
*{{cite journal |author=Belle V, Fournel A, Woudstra M, ''et al.'' |title=Probing the opening of the pancreatic lipase lid using site-directed spin labeling and EPR spectroscopy. |journal=Biochemistry |volume=46 |issue= 8 |pages= 2205–14 |year= 2007 |pmid= 17269661 |doi= 10.1021/bi0616089 }}
*{{cite journal |author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 |pmc=528928}}
*{{cite journal |author=Lowe ME |title=Structure and function of pancreatic lipase and colipase. |journal=Annu. Rev. Nutr. |volume=17 |issue= |pages= 141–58 |year= 1997 |pmid= 9240923 |doi= 10.1146/annurev.nutr.17.1.141 }}
*{{cite journal |author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2002 |pmid= 12477932 |doi= 10.1073/pnas.242603899 |pmc=139241}}
*{{cite journal |author=Bourbon-Freie A, Dub RE, Xiao X, Lowe ME |title=Trp-107 and trp-253 account for the increased steady state fluorescence that accompanies the conformational change in human pancreatic triglyceride lipase induced by tetrahydrolipstatin and bile salt. |journal=J. Biol. Chem. |volume=284 |issue= 21 |pages= 14157–64 |year= 2009 |pmid= 19346257 |doi= 10.1074/jbc.M901154200 }}
*{{cite journal |author=Ranaldi S, Belle V, Woudstra M, ''et al.'' |title=Amplitude of pancreatic lipase lid opening in solution and identification of spin label conformational subensembles by combining continuous wave and pulsed EPR spectroscopy and molecular dynamics. |journal=Biochemistry |volume=49 |issue= 10 |pages= 2140–9 |year= 2010 |pmid= 20136147 |doi= 10.1021/bi901918f }}
{{refend}}

{{PDB Gallery|geneid=5406}}
{{Esterases}}
{{Clinical biochemistry blood tests}}

[[Category:EC 3.1.1]]